1,5-Anhydroglucitol

1,5-Anhydroglucitol, also known as 1,5-AG, is a naturally occurring monosaccharide found in nearly all foods. Blood concentrations of 1,5-anhydroglucitol decrease during times of hyperglycemia above 180 mg/dL, and return to normal levels after approximately 2 weeks in the absence of hyperglycemia. As a result, it can be used for people with either type-1 or type-2 diabetes mellitus to identify glycemic variability or a history of high blood glucose even if current glycemic measurements such as hemoglobin A1c (HbA1c) and blood glucose monitoring have near normal values. Despite this possible use and its approval by the FDA, 1,5-AG tests are rarely ordered. There is some data suggesting that 1,5-AG values are useful to fill the gap and offer complementary information to HbA1c and fructosamine tests.[1]

Contents

The role of 1,5-AG was first inferred by Akanuma in 1981 [2] when he demonstrated decreased 1,5-AG levels in diabetic patients, this observation was enhanced in 1983 when it was seen that plasma 1,5-AG fell to undetectable levels in diabetic patients who did not receive insulin.[3] Further studies[4] showed that patients receiving medication to lower blood glucose had lasting improvement in 1,5-AG levels. If medication stopped, 1,5-AG decreased to pre-treatment levels; in 2003, 1,5-AG began to be looked at by researchers in the United States and was shown to be a valuable short-term glycemic monitor.[5][6] In 2006, 1,5-AG showed its most compelling clinical use when it was demonstrated that an assay (GlycoMark, developed by Nippon Kayaku, Inc.) for postprandial hyperglycemia was able to differentiate two patients who had similar, near goal, hemoglobin A1c values, yet very different glucose profiles as shown by continuous blood glucose monitoring - one of the patients having excessive glycemic variability.[7] In 2014, 1,5-AG in saliva was shown to mirror 1,5-AG in blood, indicating that it could be used as a noninvasive marker of short-term glycemic control.[8]

The assay measures blood levels of 1,5-anhydroglucitol. 1,5-AG is ingested from nearly all foods during the course of a regular diet. It is nearly 100% non metabolized and remains in a relatively constant amount in the blood and tissues. 1,5-AG is carried in the blood stream and filtered by the glomerulus, where it enters the kidney. Once in the kidney, 1,5-AG is re-absorbed back into the blood through the renal proximal tubule. A small amount, equal to the amount ingested, of 1,5-AG is released in the urine to maintain a constant amount in the blood and tissue, this process occurs in people who do not have their blood glucose values rising over 180 mg/dL.

When a diabetic person's blood glucose exceeds 180 mg/dL for any period of time, the kidney cannot re-absorb all glucose back into the blood. The rest is excreted in the urine (glucosuria), the additional glucose in the kidney blocks 1,5-AG from being re-absorbed into the blood and 1,5-AG is excreted in the urine at a higher rate than normal. Blood levels of 1,5-AG decrease immediately, and continue to decrease until glucose values go below 180 mg/dL. Once hyperglycemia is corrected, 1,5-AG begins to be re-absorbed from the kidney back into the blood at a steady rate. If a person's glucose levels remain below 180 mg/dL for approximately 4 weeks, 1,5-AG will return to its normal levels.

It is this competitive inhibition of 1,5-AG from glucose which allows the assay to accurately reflect any hyperglycemic episodes over 180 mg/dL

Reaction 2 uses pyranose oxidase to oxidize the second hydroxyl of 1,5-AG, generating hydrogen peroxide, the amount of hydrogen peroxide is detected by colorimetry using peroxidase, and is in direct relationship to the serum 1,5-AG concentration.

Results are in µg/mL. Lower values indicate worsening glucose control, with more frequent and prolonged glucose values over 180 mg/dL. 10 µg/mL of 1,5-AG correlates to an average post meal glucose of 185 mg/dL, and is the target value in people with diabetes. Values over 10 µg/mL indicate glucose on average is below 180 mg/dL. Those with values below 10 µg/mL could benefit from nutritional counseling, and medications which target post meal glucose spikes, such as pramlintide, exenatide, sitagliptin, saxagliptin, repaglinide or rapid acting insulins.

The test is cleared by the FDA to be sold and marketed for the intermediate term monitoring of glycemic control in people with diabetes. GlycoMark is available through most major reference laboratories, including Quest Diagnostics and Labcorp or may be performed in a hospital or physician's office.

1.
Monosaccharide
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Monosaccharides, also called simple sugars, are the most basic units of carbohydrates. They are fundamental units of carbohydrates and cannot be hydrolyzed to simpler compounds. The general formula is CnH 2nOn and they are the simplest form of sugar and are usually colorless, water-soluble, and crystalline solids. Some monosaccharides have a sweet taste, examples of monosaccharides include glucose, fructose and galactose. Monosaccharides are the blocks of disaccharides and polysaccharides. Further, each carbon atom that supports a group is chiral, giving rise to a number of isomeric forms. For instance, galactose and glucose are both aldohexoses, but have different physical structures and chemical properties, with few exceptions, monosaccharides have this chemical formula, Cxy, where conventionally x ≥3. Monosaccharides can be classified by the x of carbon atoms they contain, triose tetrose, pentose, hexose, heptose. The most important monosaccharide, glucose, is a hexose, examples of heptoses include the ketoses mannoheptulose and sedoheptulose. Monosaccharides with eight or more carbons are rarely observed as they are quite unstable, in aqueous solutions monosaccharides exist as rings. Simple monosaccharides have a linear and unbranched carbon skeleton with one carbonyl functional group, therefore, the molecular structure of a simple monosaccharide can be written as HnmH, where n +1 + m = x, so that its elemental formula is CxH2xOx. By convention, the atoms are numbered from 1 to x along the backbone. If the carbonyl is at position 1, the molecule begins with a formyl group H− and is technically an aldehyde, in that case, the compound is termed an aldose. Otherwise, the molecule has a group, a carbonyl −− between two carbons, then it is formally a ketone, and is termed a ketose. Ketoses of biological interest usually have the carbonyl at position 2, the various classifications above can be combined, resulting in names such as aldohexose and ketotriose. A more general nomenclature for open-chain monosaccharides combines a Greek prefix to indicate the number of carbons with the suffixes -ose for aldoses, in the latter case, if the carbonyl is not at position 2, its position is then indicated by a numeric infix. So, for example, H4H is pentose, H3H is pentulose, two monosaccharides with equivalent molecular graphs may still be distinct stereoisomers, whose molecules differ in the three-dimensional arrangement of the bonds of certain atoms. This happens only if the molecule contains a center, specifically a carbon atom that is chiral

2.
Nippon Kayaku
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Nippon Kayaku is a Japanese company that was founded in 1916 as the first industrial explosives manufacturer in Japan under the company name Nippon Kayaku Seizo Co. Ltd. Its main business areas are functional chemicals, pharmaceuticals, safety systems and it has 8 plants and 4 laboratories in Japan. It also has subsidiaries in different countries around the world and it is listed on the Nikkei 225. The company was established in 1916 to produce explosives for the construction sector, the firm then diversified into chemical dyes and pharmaceuticals in the interwar period. By 1950, Nippon Kayaku had established itself as the leading pharmaceutical firm in Japan. The launch of its drug, bleomycin, strengthened the firms pharmaceutical business

3.
Proximal tubule
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The proximal tubule is the portion of the duct system of the nephron of the kidney which leads from Bowmans capsule to the loop of Henle. It is conventionally divided into the convoluted tubule and the proximal straight tubule. The most distinctive characteristic of the tubule is its brush border. The microvilli greatly increase the surface area of the cells. The cytoplasm of the cells is densely packed with mitochondria, which are found in the basal region within the infoldings of the basal plasma membrane. The high quantity of mitochondria gives the cells an acidophilic appearance, water passively follows the sodium out of the cell along its concentration gradient. This has led observers to describe the lumen of proximal tubules as occluded or dirty-looking, in contrast to the clean appearance of distal tubules. The proximal tubule as a part of the nephron can be divided into two sections, pars convoluta and pars recta, differences in cell outlines exist between these segments, and therefore presumably in function too. Regarding ultrastructure, it can be divided into three segments, oS1, S2, and S3, The pars convoluta is the initial convoluted portion. In relation to the morphology of the kidney as a whole, some investigators on the basis of particular functional differences have divided the convoluted part into two segments designated S1 and S2. The pars recta is the straight portion. Straight segments descend into the outer medulla and they terminate at a remarkably uniform level and it is their line of termination that establishes the boundary between the inner and outer stripes of the outer zone of the renal medulla. As a logical extension of the described above, this segment is sometimes designated as S3. Fluid in the entering the proximal convoluted tubule is reabsorbed into the peritubular capillaries. This is driven by sodium transport from the lumen into the blood by the Na+/K+ ATPase in the membrane of the epithelial cells. Sodium reabsorption is primarily driven by this P-type ATPase and this is the most important transport mechanism in the PCT. Many types of medications are secreted in the proximal tubule, further reading, Table of medication secreted in kidney Most of the ammonium that is excreted in the urine is formed in the proximal tubule via the breakdown of glutamine to alpha-ketoglutarate. This takes place in two steps, each of which generates an ammonium anion, the conversion of glutamine to glutamate, proximal tubular epithelial cells have a pivotal role in kidney disease

4.
Glucokinase
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Glucokinase is an enzyme that facilitates phosphorylation of glucose to glucose-6-phosphate. Glucokinase occurs in cells in the liver and pancreas of humans, mutations of the gene for this enzyme can cause unusual forms of diabetes or hypoglycemia. Glucokinase is a hexokinase isozyme, related homologously to at least three other hexokinases, all of the hexokinases can mediate phosphorylation of glucose to glucose-6-phosphate, which is the first step of both glycogen synthesis and glycolysis. However, glucokinase is coded by a gene and its distinctive kinetic properties allow it to serve a different set of functions. Because of this reduced affinity, the activity of glucokinase, under physiological conditions. Alternative names for this enzyme are, human hexokinase IV, hexokinase D, the common name, glucokinase, is derived from its relative specificity for glucose under physiologic conditions.7.1.2. Nevertheless, glucokinase remains the name preferred in the contexts of medicine, another mammalian glucose kinase, ADP-specific glucokinase, was discovered in 2004. The gene is distinct and similar to that of primitive organisms and it is dependent on ADP rather than ATP, and the metabolic role and importance remain to be elucidated. The principal substrate of physiologic importance of glucokinase is glucose, the other necessary substrate, from which the phosphate is derived, is adenosine triphosphate, which is converted to adenosine diphosphate when the phosphate is removed. The reaction catalyzed by glucokinase is, ATP participates in the reaction in a form complexed to magnesium as a cofactor, furthermore, under certain conditions, glucokinase, like other hexokinases, can induce phosphorylation of other hexoses and similar molecules. Two important kinetic properties distinguish glucokinase from the other hexokinases, allowing it to function in a role as glucose sensor. Glucokinase has an affinity for glucose than the other hexokinases. Glucokinase changes conformation and/or function in parallel with rising glucose concentrations in the physiologically important range of 4–10 mmol/L and it is half-saturated at a glucose concentration of about 8 mmol/L. Glucokinase is not inhibited by its product, glucose-6-phosphate and this allows continued signal output amid significant amounts of its product These two features allow it to regulate a supply-driven metabolic pathway. That is, the rate of reaction is driven by the supply of glucose, another distinctive property of glucokinase is its moderate cooperativity with glucose, with a Hill coefficient of about 1.7. Glucokinase has only a binding site for glucose and is the only monomeric regulatory enzyme known to display substrate cooperativity. The nature of the cooperativity has been postulated to involve a transition between two different enzyme states with different rates of activity. If the dominant state depends upon glucose concentration, it would produce an apparent cooperativity similar to that observed, because of this cooperativity, the kinetic interaction of glucokinase with glucose does not follow classical Michaelis-Menten kinetics

5.
Adenosine triphosphate
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Adenosine triphosphate is a nucleotide, also called a nucleoside triphosphate, is a small molecule used in cells as a coenzyme. It is often referred to as the unit of currency of intracellular energy transfer. ATP transports chemical energy within cells for metabolism, most cellular functions need energy in order to be carried out, synthesis of proteins, synthesis of membranes, movement of the cell, cellular division, transport of various solutes etc. The ATP is the molecule that carries energy to the place where the energy is needed, when ATP breaks into ADP and Pi, the breakdown of the last covalent link of phosphate liberates energy that is used in reactions where it is needed. Substrate-level phosphorylation, oxidative phosphorylation in cellular respiration, and photophosphorylation in photosynthesis are three mechanisms of ATP biosynthesis. Metabolic processes that use ATP as an energy source convert it back into its precursors, ATP is therefore continuously recycled in organisms, the human body, which on average contains only 250 grams of ATP, turns over its own body weight equivalent in ATP each day. ATP is used as a substrate in signal transduction pathways by kinases that phosphorylate proteins and it is also used by adenylate cyclase, which uses ATP to produce the second messenger molecule cyclic AMP. The ratio between ATP and AMP is used as a way for a cell to sense how much energy is available and control the metabolic pathways that produce and consume ATP. Apart from its roles in signaling and energy metabolism, ATP is also incorporated into nucleic acids by polymerases in the process of transcription, ATP is the neurotransmitter believed to signal the sense of taste. The structure of this consists of a purine base attached by the 9′ nitrogen atom to the 1′ carbon atom of a pentose sugar. Three phosphate groups are attached at the 5′ carbon atom of the pentose sugar and it is the addition and removal of these phosphate groups that inter-convert ATP, ADP and AMP. When ATP is used in DNA synthesis, the sugar is first converted to deoxyribose by ribonucleotide reductase. ATP was discovered in 1929 by Karl Lohmann, and independently by Cyrus Fiske and Yellapragada Subbarow of Harvard Medical School and it was proposed to be the intermediary molecule between energy-yielding and energy-requiring reactions in cells by Fritz Albert Lipmann in 1941. It was first artificially synthesized by Alexander Todd in 1948, ATP consists of adenosine – composed of an adenine ring and a ribose sugar – and three phosphate groups. The phosphoryl groups, starting with the group closest to the ribose, are referred to as the alpha, beta, consequently, it is closely related to the adenosine nucleotide, a monomer of RNA. ATP is highly soluble in water and is stable in solutions between pH6.8 and 7.4, but is rapidly hydrolysed at extreme pH. Consequently, ATP is best stored as an anhydrous salt, ATP is an unstable molecule in unbuffered water, in which it hydrolyses to ADP and phosphate. This is because the strength of the bonds between the groups in ATP is less than the strength of the hydrogen bonds, between its products, and water

6.
Pyruvate kinase
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Pyruvate kinase is the enzyme that catalyzes the final step of glycolysis. It catalyzes the transfer of a group from phosphoenolpyruvate to adenosine diphosphate, yielding one molecule of pyruvate. There are four isozymes of pyruvate kinase in vertebrates, L, R, M1, R and L isozymes differ from M1 and M2 in that they are both exclusively allosterically and reversibly regulated. From a kinetic standpoint, the R and L isozymes of pyruvate kinase have two key conformation states, one with a high affinity and one with a low substrate affinity. The R-state, characterized by high affinity, serves as the activated form of pyruvate kinase and is stabilized by PEP and FBP. Gene expression varies between the different isozymes, M1 and M2 isozymes are regulated by the gene PKM and R and L isozymes are regulated by the gene PKLR. In terms of structure, there is both a tetrameric and dimeric form of pyruvate kinase, the tetrameric form is the pyruvate kinase structure in its R-state conformation, namely with high binding affinity to PEP. In contrast, the form is its structure in T-state conformation. Many Enterobacteriaceae, including E. coli, have two isoforms of pyruvate kinase, PykA and PykF, which are 37% identical in E. coli. They catalyze the reaction as in eukaryotes, namely the generation of ATP from ADP and PEP, the last step in glycolysis. PykF is allosterically regulated by fructose 1, 6-bisphosphate which reflects the position of PykF in cellular metabolism. PykF transcription in E. coli is regulated by the transcriptional regulator. PfkB was shown to be inhibited by MgATP at low concentrations of Fru-6P, there are two steps in the pyruvate kinase reaction in glycolysis. First, PEP transfers a phosphate group to ADP, producing ATP, secondly, a proton must be added to the enolate of pyruvate to produce the functional form of pyruvate that the cell requires. In yeast cells, the interaction of yeast pyruvate kinase with PEP and its allosteric effector Fructose 1, therefore, Mg2+ was isolated as an important component in the successful catalysis of PEP into pyruvate by pyruvate kinase. Furthermore, the metal ion Mn2+ was shown to have a similar, the binding of metal ions to the metal binding sites on pyruvate kinase enhance the rate of this glycolytic reaction. The glycolytic reaction catalyzed by pyruvate kinase is the step of glycolysis. It is one of the three rate-affecting steps of the catabolic reaction cascade, the rate-affecting steps are the slower steps of a reaction and thus determines the rate of the overall reaction

7.
Phosphoenolpyruvic acid
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Phosphoenolpyruvic acid, or phosphoenolpyruvate as the anion, is an important chemical compound in biochemistry. It has the highest-energy phosphate bond found in living organisms, and is involved in glycolysis and gluconeogenesis. In plants, it is involved in the biosynthesis of various aromatic compounds. PEP is formed by the action of the enzyme enolase on 2-phosphoglyceric acid, metabolism of PEP to pyruvic acid by pyruvate kinase generates 1 molecule of adenosine triphosphate via substrate-level phosphorylation. ATP is one of the currencies of chemical energy within cells. Compound C00631 at KEGG Pathway Database, enzyme 4.2.1.11 at KEGG Pathway Database. Compound C00074 at KEGG Pathway Database, enzyme 2.7.1.40 at KEGG Pathway Database. Compound C00022 at KEGG Pathway Database, PEP is formed from the decarboxylation of oxaloacetate and hydrolysis of one guanosine triphosphate molecule. This reaction is catalyzed by the enzyme phosphoenolpyruvate carboxykinase and this reaction is a rate-limiting step in gluconeogenesis, GTP + oxaloacetate → GDP + phosphoenolpyruvate + CO2 Click on genes, proteins and metabolites below to link to respective articles. PEP may be used for the synthesis of chorismate through the shikimate pathway, chorismate may then be metabolized into the aromatic amino acids and other aromatic compounds. The first step is when Phosphoenolpyruvate and erythrose-4-phosphate react to form 3-deoxy-D-arabinoheptulosonate-7-phosphate, in addition, in C4 plants, PEP serves as an important substrate in carbon fixation. The chemical equation, as catalyzed by phosphoenolpyruvate carboxylase, is, PEP + HCO3− → oxaloacetate

8.
Hydrogen peroxide
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Hydrogen peroxide is a chemical compound with the formula H 2O2. In its pure form, it is a liquid, slightly more viscous than water. Hydrogen peroxide is the simplest peroxide and it is used as an oxidizer, bleaching agent and disinfectant. Concentrated hydrogen peroxide, or high-test peroxide, is an oxygen species and has been used as a propellant in rocketry. Its chemistry is dominated by the nature of its unstable peroxide bond, Hydrogen peroxide is unstable and slowly decomposes in the presence of base or a catalyst. Because of its instability, hydrogen peroxide is typically stored with a stabilizer in an acidic solution. Hydrogen peroxide is found in biological systems including the human body, enzymes that use or decompose hydrogen peroxide are classified as peroxidases. The boiling point of H 2O2 has been extrapolated as being 150.2 °C, in practice hydrogen peroxide will undergo potentially explosive thermal decomposition if heated to this temperature. It may be distilled at lower temperatures under reduced pressure. In aqueous solutions hydrogen peroxide differs from the material due to the effects of hydrogen bonding between water and hydrogen peroxide molecules. Hydrogen peroxide and water form a mixture, exhibiting freezing-point depression, pure water has a melting point of 0 °C. The boiling point of the same mixtures is also depressed in relation with the mean of both boiling points and this boiling point is 14 °C greater than that of pure water and 36.2 °C less than that of pure hydrogen peroxide. Hydrogen peroxide is a molecule with C2 symmetry. Although the O−O bond is a bond, the molecule has a relatively high rotational barrier of 2460 cm−1, for comparison. The increased barrier is ascribed to repulsion between the pairs of the adjacent oxygen atoms and results in hydrogen peroxide displaying atropisomerism. The molecular structures of gaseous and crystalline H 2O2 are significantly different and this difference is attributed to the effects of hydrogen bonding, which is absent in the gaseous state. Crystals of H 2O2 are tetragonal with the space group D4 4P4121, Hydrogen peroxide has several structural analogues with Hm−X−X−Hn bonding arrangements. It has the highest boiling point of this series, diphosphane and hydrogen disulfide exhibit only weak hydrogen bonding and have little chemical similarity to hydrogen peroxide

9.
Peroxidase
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Peroxidases can contain a heme cofactor in their active sites, or alternately redox-active cysteine or selenocysteine residues. The nature of the donor is very dependent on the structure of the enzyme. For example, horseradish peroxidase can use a variety of compounds as electron donors and acceptors. Horseradish peroxidase has an active site, and many compounds can reach the site of the reaction. Because there is a very closed active site, for a such as cytochrome c peroxidase. While the exact mechanisms have yet to be determined, peroxidases are known to play a part in increasing a plants defenses against pathogens, peroxidases are sometimes used as histological marker. Cytochrome c peroxidase is used as a soluble, easily purified model for cytochrome c oxidase, the glutathione peroxidase family consists of 8 known human isoforms. Glutathione peroxidases use glutathione as a donor and are active with both hydrogen peroxide and organic hydroperoxide substrates. Gpx1, Gpx2, Gpx3, and Gpx4 have been shown to be selenium-containing enzymes, amyloid beta, when bound to heme, has been shown to have peroxidase activity. A typical group of peroxidases are the haloperoxidases and this group is able to form reactive halogen species and, as a result, natural organohalogen substances. A majority of protein sequences can be found in the PeroxiBase database. Peroxidase can be used for treatment of waste waters. For example, phenols, which are important pollutants, can be removed by enzyme-catalyzed polymerization using horseradish peroxidase, thus phenols are oxidized to phenoxy radicals, which participate in reactions where polymers and oligomers are produced that are less toxic than phenols. It also can be used to convert toxic materials into less harmful substances, there are many investigations about the use of peroxidase in many manufacturing processes like adhesives, computer chips, car parts, and linings of drums and cans. Other studies have shown that peroxidases may be used successfully to polymerize anilines and phenols in organic solvent matrices

10.
Quest Diagnostics
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Quest Diagnostics Incorporated is a Fortune 500 company providing clinical laboratory services with headquarters in Madison, New Jersey. Founded in 1967 as Metropolitan Pathology Laboratory, Inc. it became an independent corporation with the Quest name on December 31,1996 and it is a member of the Fortune 500 and the S&P500, with corporate headquarters located in Madison, New Jersey. 1967, Founded by Paul A. Brown, MD as Metropolitan Pathology Laboratory,1969, Name Changed to MetPath, Inc. in Teaneck, New Jersey. 1982, MetPath was acquired by what was known as Corning Glass Works. 1996, Quest Diagnostics becomes an independent company as a spin-off from Corning,1997, Acquires clinical laboratory division of Branford, CT-based Diagnostic Medical Laboratory, Inc. 1999, Acquires SmithKline Beecham Clinical Laboratories, GlaxoSmithKline still holds a portion of Quest Diagnostics stock. 2002, Completes acquisition of Virginia-based American Medical Laboratories, Inc.2003, Completes acquisition of California-based Unilab Corporation in a transaction valued at approximately $800 million. 2005, Completes acquisition of Kansas-based LabOne, Inc. for approximately $934 million,2005, forms a strategic alliance with Ciphergen Biosystems to commercialize novel proteomic tests. 2006, Completes acquisition of Virginia-based Focus Diagnostics, Inc. an infectious and immunologic disease laboratory,2007, Completes acquisition of Sweden-based Hemocue, a point-of-care diagnostic testing company. 2007, Acquires AmeriPath from Welsh, Carson, Anderson & Stowe,2011, Acquires Athena Diagnostics from Thermo Fisher Scientific 2011, Completes acquisition of Celera Corporation, a company that became famous by its sequencing of the Human Genome. 2012, Names former Philips Healthcare CEO Stephen Rusckowski as CEO,2012, CEO, Surya Mohapatra, PhD resigns after leading the company for 8 years 2012, Quest Diagnostics bought all the labs including the business from UMASS Memorial Hospitals in Worcester, MA. 2014, Acquires Solstas Lab Partners Group 2014, Acquires Summit Health, Quest Diagnostics set a record in April 2009 when it paid $302 million to the government to settle a Medicare fraud case alleging the company sold faulty medical testing kits. It was the largest qui tam settlement paid by a lab for manufacturing and distributing a faulty product

11.
Labcorp
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Laboratory Corporation of America Holdings, more commonly known as LabCorp, is an American S&P500 company headquartered in Burlington, North Carolina. It operates one of the largest clinical laboratory networks in the world, before a merger with National Health Laboratory in 1995, the company operated under the name Roche BioMedical. LabCorp performs its largest volume of specialty testing at its Center for Esoteric Testing in Burlington, North Carolina and it also does oncology testing, human immunodeficiency virus genotyping and phenotyping. LabCorp also operates the National Genetics Institute, Inc. in Los Angeles, LabCorp also provides testing in Puerto Rico and, outside the United States, in three Canadian provinces. LabCorp Utilizes 7 PA-31-350s and 1 PC-12 aircraft on nightly runs from Burlington, LabCorp has been criticized for its practice of paying the salaries of genetic counselors in hospitals and doctors offices, which is perceived to be a possible conflict of interest. National Health Laboratories Incorporated began in 1978, the company was a national blood and pathology laboratory owned by the Revlon Health Care Group, and managed by Michael E. Lillig for seven years. Lillig had earlier been with Becton, Dickinson and Company, at National Health Laboratories, Inc. he grew annual sales of the company each year by 43%, with revenue reaching $12 million by the end of his tenure. Lillig then left to found several companies, including Syscor. Asterion, LLC and MetaCytes 3DR in Louisville, Kentucky, in 1988, National Health Laboratories became publicly traded on the NASDAQ exchange. Revlon retained 24% ownership of the shares, for the next six years. Revlon had been a traded company since the 1950s, as it was during most of its ownership of National Health Laboratories. But in 1985, Revlon had been taken over by Ronald Perelman, through early 1995, the National Health Laboratories principal executive offices were located at 4225 Executive Square, Suite 805 in La Jolla, California. In 1989, the generated revenue of about US$400 million. In 1990, the companys revenues reached US$500 million, with over US$70 million in earnings and that year, the company began paying a cash dividend to shareholders. In 1991, National Health Laboratories moved from the NASDAQ OTC exchange to the New York Stock Exchange, up until that time the company had performed very well, including through the 1990-1991 recession. Its earnings peaked that year at almost US$90 million, and its price had risen from its low within the prior few years by several-fold. The charges were that the company and others routinely submitted false claims to the government health-care agencies Medicare, in 1992, National Health Laboratories became the first of the companies to be prosecuted in the government operation. In 1992, the company reported revenues of over US$720 million, the small gain that year reflected a fourth quarter charge of US$80 million, which the company paid in a settlement agreement with state and federal governments related to the LABSCAM investigation

12.
PubMed Identifier
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PubMed is a free search engine accessing primarily the MEDLINE database of references and abstracts on life sciences and biomedical topics. The United States National Library of Medicine at the National Institutes of Health maintains the database as part of the Entrez system of information retrieval, from 1971 to 1997, MEDLINE online access to the MEDLARS Online computerized database primarily had been through institutional facilities, such as university libraries. PubMed, first released in January 1996, ushered in the era of private, free, home-, the PubMed system was offered free to the public in June 1997, when MEDLINE searches via the Web were demonstrated, in a ceremony, by Vice President Al Gore. Information about the journals indexed in MEDLINE, and available through PubMed, is found in the NLM Catalog. As of 5 January 2017, PubMed has more than 26.8 million records going back to 1966, selectively to the year 1865, and very selectively to 1809, about 500,000 new records are added each year. As of the date,13.1 million of PubMeds records are listed with their abstracts. In 2016, NLM changed the system so that publishers will be able to directly correct typos. Simple searches on PubMed can be carried out by entering key aspects of a subject into PubMeds search window, when a journal article is indexed, numerous article parameters are extracted and stored as structured information. Such parameters are, Article Type, Secondary identifiers, Language, publication type parameter enables many special features. As these clinical girish can generate small sets of robust studies with considerable precision, since July 2005, the MEDLINE article indexing process extracts important identifiers from the article abstract and puts those in a field called Secondary Identifier. The secondary identifier field is to store numbers to various databases of molecular sequence data, gene expression or chemical compounds. For clinical trials, PubMed extracts trial IDs for the two largest trial registries, ClinicalTrials. gov and the International Standard Randomized Controlled Trial Number Register, a reference which is judged particularly relevant can be marked and related articles can be identified. If relevant, several studies can be selected and related articles to all of them can be generated using the Find related data option, the related articles are then listed in order of relatedness. To create these lists of related articles, PubMed compares words from the title and abstract of each citation, as well as the MeSH headings assigned, using a powerful word-weighted algorithm. The related articles function has been judged to be so precise that some researchers suggest it can be used instead of a full search, a strong feature of PubMed is its ability to automatically link to MeSH terms and subheadings. Examples would be, bad breath links to halitosis, heart attack to myocardial infarction, where appropriate, these MeSH terms are automatically expanded, that is, include more specific terms. Terms like nursing are automatically linked to Nursing or Nursing and this important feature makes PubMed searches automatically more sensitive and avoids false-negative hits by compensating for the diversity of medical terminology. The My NCBI area can be accessed from any computer with web-access, an earlier version of My NCBI was called PubMed Cubby

13.
Blood sugar level
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The blood sugar concentration or blood glucose level is the amount of glucose present in the blood of a human or animal. The body naturally tightly regulates blood glucose levels as a part of metabolic homeostasis, with some exceptions, glucose is the primary source of energy for the bodys cells, and blood lipids are primarily a compact energy store. Glucose levels are usually lowest in the morning, before the first meal of the day, Blood sugar levels outside the normal range may be an indicator of a medical condition. A persistently high level is referred to as hyperglycemia, low levels are referred to as hypoglycemia, Diabetes mellitus is characterized by persistent hyperglycemia from any of several causes, and is the most prominent disease related to failure of blood sugar regulation. Intake of alcohol causes a surge in blood sugar. Also, certain drugs can increase or decrease glucose levels, the international standard way of measuring blood glucose levels are in terms of a molar concentration, measured in mmol/L. In the United States, West-Germany and other countries mass concentration is measured in mg/dL, since the molecular weight of glucose C6H12O6 is 180, the difference between the two units is a factor of 18, so that 1 mmol/L of glucose is equivalent to 18 mg/dL. Normal value ranges may vary slightly among different laboratories, many factors affect a persons blood sugar level. A bodys homeostatic mechanism, when operating normally, restores the blood sugar level to a range of about 4.4 to 6.1 mmol/L. The normal blood level for non-diabetics, should be between 3.9 and 5.5 mmol/L. The mean normal blood glucose level in humans is about 5.5 mmol/L, however, Blood sugar levels for those without diabetes and who are not fasting should be below 6.9 mmol/L. The blood glucose target range for diabetics, according to the American Diabetes Association, should be 5. 0–7.2 mmol/l before meals, and less than 10 mmol/L after meals. Despite widely variable intervals between meals or the consumption of meals with a substantial carbohydrate load, human blood glucose levels tend to remain within the normal range. However, shortly after eating, the glucose level may rise, in non-diabetics. The actual amount of glucose in the blood and body fluids is very small. In a healthy adult male of 75 kg with a volume of 5 liters. Part of the reason why this amount is so small is that, to maintain an influx of glucose into cells, in general, ranges of blood sugar in common domestic ruminants are lower than in many monogastric mammals. However this generalization does not extend to wild ruminants or camelids, a 90 percent reference interval for serum glucose of 26 to 181 mg/dL has been reported for captured mountain goats, where no effects of the pursuit and capture on measured levels were evident

Paramedics in Southern California attend a diabetic man who lost effective control of his vehicle due to low blood sugar (hypoglycemia) and drove it over the curb and into the water main and backflow valve in front of this industrial building. He was not injured, but required emergency intravenous glucose.

The Insulin pump is used to automatically deliver basalinsulin continuously, and bolus insulin at meal times by pressing the buttons. Before meals, a blood glucose value is entered into the pump to calculate the correction bolus to bring the blood glucose level back to the target value.